USP7 is a SUMO deubiquitinase essential for DNA replication.

Universal sample preparation method for proteome analysis

Wiśniewski, J. R., Zougman, A., Nagaraj, N., & Mann, M. (2009) · Nature Methods · doi:10.1038/nmeth.1322 · Cited by 8,352 · see citing works

Stop and Go Extraction Tips for Matrix-Assisted Laser Desorption/Ionization, Nanoelectrospray, and LC/MS Sample Pretreatment in Proteomics

Rappsilber, J., Ishihama, Y., & Mann, M. (2002) · Analytical Chemistry · doi:10.1021/ac026117i · Cited by 2,589 · see citing works

Systematic and Quantitative Assessment of the Ubiquitin-Modified Proteome

Kim, W., Bennett, E. J., Huttlin, E. L., Guo, A., Li, J., Possemato, A. P., Sowa, M. E., Rad, R., Rush, A. J., Comb, M. J., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.025 · Cited by 1,582 · see citing works

Defining the Human Deubiquitinating Enzyme Interaction Landscape

Sowa, M. E., Bennett, E. J., Gygi, S. P., & Harper, J. W. (2009) · Cell · doi:10.1016/j.cell.2009.04.042 · Cited by 1,512 · see citing works

Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization

Li, M., Chen, D., Shiloh, A., Luo, J., Nikolaev, A. Y., Qin, J., & Gu, W. J. (2002) · Nature · doi:10.1038/nature737 · Cited by 1,027 · see citing works

Chromatin Association of Human Origin Recognition Complex, Cdc6, and Minichromosome Maintenance Proteins during the Cell Cycle: Assembly of Prereplication Complexes in Late Mitosis

Méndez, J., & Stillman, B. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.22.8602-8612.2000 · Cited by 918 · see citing works

Replicon Clusters Are Stable Units of Chromosome Structure: Evidence That Nuclear Organization Contributes to the Efficient Activation and Propagation of S Phase in Human Cells

Jackson, D., & Pombo, A. (1998) · Journal of Cell Biology · doi:10.1083/jcb.140.6.1285 · Cited by 881 · see citing works

PCGF Homologs, CBX Proteins, and RYBP Define Functionally Distinct PRC1 Family Complexes

Gao, Z., Zhang, J., Bonasio, R., Strino, F., Sawai, A., Parisi, F., Kluger, Y., & Reinberg, D. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.01.002 · Cited by 852 · see citing works

RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation

Tatham, M. H., Geoffroy, M., Shen, L., Plechanovová, A., Hattersley, N., Jaffray, E., Palvimo, J. J., & Hay, R. T. (2008) · Nature Cell Biology · doi:10.1038/ncb1716 · Cited by 837 · see citing works

Hydroxyurea-Stalled Replication Forks Become Progressively Inactivated and Require Two Different RAD51-Mediated Pathways for Restart and Repair

Petermann, E., Orta, M. L., Issaeva, N., Schultz, N., & Helleday, T. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.021 · Cited by 815 · see citing works

A dynamic role of HAUSP in the p53-Mdm2 pathway

Li, M., Brooks, C. L., Kon, N., & Gu, W. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00157-1 · Cited by 679 · see citing works

Dormant origins licensed by excess Mcm2–7 are required for human cells to survive replicative stressPreprint

Ge, X. Q., Jackson, D. A., & Blow, J. J. (2007) · Genes & Development · doi:10.1101/gad.457807 · Cited by 605 · see citing works

A small molecule inhibitor of ubiquitin-specific protease-7 induces apoptosis in multiple myeloma cells and overcomes bortezomib resistance.

Chauhan, D., Tian, Z., Nicholson, B., Kumar, K. G. S., Zhou, B., Carrasco, R., McDermott, J. L., Leach, C. A., Fulcinniti, M., Kodrasov, M. P., et al. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.08.007 · Cited by 589 · see citing works

The Deubiquitinating Enzyme USP1 Regulates the Fanconi Anemia Pathway

Nijman, S. M. B., Huang, T. T., Dirac, A. M. G., Brummelkamp, T. R., Kerkhoven, R. M., D’Andrea, A. D., & Bernards, R. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.01.008 · Cited by 586 · see citing works

Regulation of monoubiquitinated PCNA by DUB autocleavage

Huang, T. T., Nijman, S. M. B., Mirchandani, K. D., Galardy, P. J., Cohn, M. A., Haas, W., Gygi, S. P., Ploegh, H. L., Bernards, R., & D’Andrea, A. D. (2006) · Nature Cell Biology · doi:10.1038/ncb1378 · Cited by 585 · see citing works

The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network

Song, M. S., Salmena, L., Carracedo, A., Egia, A., Lo-Coco, F., Teruya-Feldstein, J., & Pandolfi, P. P. (2008) · Nature · doi:10.1038/nature07290 · Cited by 548 · see citing works

Combination of FASP and StageTip-based fractionation allows in-depth analysis of the hippocampal membrane proteome

Wiśniewski, J. R., Zougman, A., & Mann, M. (2009) · Journal of Proteome Research · doi:10.1021/pr900748n · Cited by 545 · see citing works

Excess MCM proteins protect human cells from replicative stress by licensing backup origins of replication

Ibarra, A., Schwob, É., & Méndez, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803978105 · Cited by 505 · see citing works

System-Wide Changes to SUMO Modifications in Response to Heat Shock

Gołębiowski, F., Matić, I., Tatham, M. H., Cole, C., Yin, Y., Nakamura, A., Cox, J., Barton, G. J., Mann, M., & Hay, R. T. (2009) · Science Signaling · doi:10.1126/scisignal.2000282 · Cited by 485 · see citing works

Protein Group Modification and Synergy in the SUMO Pathway as Exemplified in DNA Repair

Psakhye, I., & Jentsch, S. (2012) · Cell · doi:10.1016/j.cell.2012.10.021 · Cited by 484 · see citing works

FOXO4 transcriptional activity is regulated by monoubiquitination and USP7/HAUSP

van der Horst, A., de Vries-Smits, A. M. M., Brenkman, A. B., van Triest, M. H., van den Broek, N. J. F., Colland, F., Maurice, M. M., & Burgering, B. M. T. (2006) · Nature Cell Biology · doi:10.1038/ncb1469 · Cited by 479 · see citing works

A cell-based screen identifies ATR inhibitors with synthetic lethal properties for cancer-associated mutations

Toledo, L. I., Murga, M., Zur, R., Soria, R., Rodriguez, A., Martinez, S., Oyarzabal, J., Pastor, J., Bischoff, J. R., & Fernandez-Capetillo, O. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2076 · Cited by 465 · see citing works

ATM-mediated stabilization of ZEB1 promotes DNA damage response and radioresistance through CHK1

Zhang, P., Wei, Y., Wang, L., Debeb, B. G., Yuan, Y., Zhang, J., Yuan, J., Wang, M., Chen, D., Sun, Y., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb3013 · Cited by 454 · see citing works

Analysis of protein dynamics at active, stalled, and collapsed replication forksPreprint

Sirbu, B. M., Couch, F. B., Feigerle, J. T., Bhaskara, S., Hiebert, S. W., & Cortez, D. (2011) · Genes & Development · doi:10.1101/gad.2053211 · Cited by 430 · see citing works

Activity-Based Chemical Proteomics Accelerates Inhibitor Development for Deubiquitylating Enzymes

Altun, M., Kramer, H., Willems, L. I., McDermott, J. L., Leach, C. A., Goldenberg, S. J., Kumar, S., Konietzny, R., Fischer, R., Kogan, E., et al. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.08.018 · Cited by 401 · see citing works

Disruption of HAUSP gene stabilizes p53.

Cummins, J. M., Rago, C., Kohli, M., Kinzler, K. W., Lengauer, C., & Vogelstein, B. (2004) · Nature · doi:10.1038/nature02501 · Cited by 379 · see citing works

The Replication Checkpoint Prevents Two Types of Fork Collapse without Regulating Replisome Stability

Dungrawala, H., Rose, K. L., Bhat, K. P., Mohni, K. N., Glick, G. G., Couch, F. B., & Cortez, D. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.07.030 · Cited by 376 · see citing works

Covalent and allosteric inhibitors of the ATPase VCP/p97 induce cancer cell death

Magnaghi, P., D’Alessio, R., Valsasina, B., Avanzi, N. R., Rizzi, S., Asa, D., Gasparri, F., Cozzi, L., Cucchi, U., Orrenius, C., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1313 · Cited by 369 · see citing works

A UAF1-Containing Multisubunit Protein Complex Regulates the Fanconi Anemia Pathway

Cohn, M. A., Kowal, P., Yang, K., Haas, W., Huang, T. T., Gygi, S. P., & D’Andrea, A. D. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.09.031 · Cited by 355 · see citing works

DNMT1 Stability Is Regulated by Proteins Coordinating Deubiquitination and Acetylation-Driven Ubiquitination

Du, Z., Song, J. K., Wang, Y., Zhao, Y., Guda, K., Yang, S., Kao, H., Xu, Y., Willis, J. E., Markowitz, S. D., et al. (2010) · Science Signaling · doi:10.1126/scisignal.2001462 · Cited by 337 · see citing works

Chromatin Dynamics During DNA Replication and Uncharacterized Replication Factors determined by Nascent Chromatin Capture (NCC) Proteomics

Alabert, C., Bukowski-Wills, J.-C., Lee, S.-B., Kustatscher, G., Nakamura, K., Alves, F. D. L., Ménard, P., Mejlvang, J., Rappsilber, J., & Groth, A. (2014) · Nature Cell Biology · doi:10.1038/ncb2918 · Cited by 334 · see citing works

Repriming of DNA synthesis at stalled replication forks by human PrimPol

Mouron, S. A., Rodríguez‐Acebes, S., Martínez-Jiménez, M. I., García-Gómez, S., Chocrón, S., Blanco, L., & Méndez, J. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2719 · Cited by 322 · see citing works

RNF4, a SUMO-targeted ubiquitin E3 ligase, promotes DNA double-strand break repair

Galanty, Y., Belotserkovskaya, R., Coates, J., & Jackson, S. P. (2012) · Genes & Development · doi:10.1101/gad.188284.112 · Cited by 314 · see citing works

Chk1 promotes replication fork progression by controlling replication initiation

Petermann, E., Woodcock, M., & Helleday, T. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1005031107 · Cited by 308 · see citing works

Large-scale identification of ubiquitination sites by mass spectrometry

Udeshi, N. D., Mertins, P., Svinkina, T., & Carr, S. A. (2013) · Nature Protocols · doi:10.1038/nprot.2013.120 · Cited by 299 · see citing works

Deregulation of cyclin E in human cells interferes with prereplication complex assembly

Ekholm‐Reed, S., Méndez, J., Tedesco, D., Zetterberg, A., Stillman, B., & Reed, S. I. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200404092 · Cited by 296 · see citing works

UV-sensitive syndrome protein UVSSA recruits USP7 to regulate transcription-coupled repair

Schwertman, P., Lagarou, A., Dekkers, D. H. W., Raams, A., van der Hoek, A. C., Laffeber, C., Hoeijmakers, J. H. J., Demmers, J. A. A., Fousteri, M., Vermeulen, W., et al. (2012) · Nature Genetics · doi:10.1038/ng.2230 · Cited by 279 · see citing works

Discovery of specific inhibitors of human USP7/HAUSP deubiquitinating enzyme.

Reverdy, C., Conrath, S., Lopez, R., Planquette, C., Atmanene, C., Collura, V., Harpon, J., Battaglia, V., Vivat, V., Sippl, W., et al. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.02.007 · Cited by 270 · see citing works

A selective USP1–UAF1 inhibitor links deubiquitination to DNA damage responses

Liang, Q., Dexheimer, T. S., Zhang, P., Rosenthal, A. S., Villamil, M. A., You, C., Zhang, Q., Chen, J., Ott, C. A., Sun, H., et al. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1455 · Cited by 264 · see citing works

SUMO-targeted ubiquitin ligases

Sriramachandran, A. M., & Dohmen, R. J. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.08.022 · Cited by 241 · see citing works

SUMO-targeted ubiquitin E3 ligase RNF4 is required for the response of human cells to DNA damage

Yin, Y., Seifert, A., Chua, J. S., Maure, J.-F., Golebiowski, F., & Hay, R. T. (2012) · Genes & Development · doi:10.1101/gad.189274.112 · Cited by 237 · see citing works

Mechanism of CRL4Cdt2, a PCNA-dependent E3 ubiquitin ligasePreprint

Havens, C. G., & Walter, J. C. (2011) · Genes & Development · doi:10.1101/gad.2068611 · Cited by 223 · see citing works

Proteome-Wide Identification of SUMO2 Modification Sites

Tammsalu, T., Matić, I., Jaffray, E., Ibrahim, A. F. M., Tatham, M. H., & Hay, R. T. (2014) · Science Signaling · doi:10.1126/scisignal.2005146 · Cited by 209 · see citing works

The USP7/Dnmt1 complex stimulates the DNA methylation activity of Dnmt1 and regulates the stability of UHRF1

Felle, M., Joppien, S., Németh, A., Diermeier, S. D., Thalhammer, V., Dobner, T., Kremmer, E., Kappler, R., & Längst, G. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr528 · Cited by 198 · see citing works

Selective dual inhibitors of the cancer-related deubiquitylating proteases USP7 and USP47.

Weinstock, J., Wu, J., Cao, P., Kingsbury, W. D., McDermott, J. L., Kodrasov, M. P., McKelvey, D. M., Suresh Kumar, K. G., Goldenberg, S. J., Mattern, M. R., et al. (2012) · ACS Medicinal Chemistry Letters · doi:10.1021/ml200276j · Cited by 187 · see citing works

Inactivation of HAUSP in vivo modulates p53 function.

Kon, N., Kobayashi, Y., Li, M., Brooks, C. L., Ludwig, T., & Gu, W. (2010) · Oncogene · doi:10.1038/onc.2009.427 · Cited by 176 · see citing works

DVC1 (C1orf124) is a DNA damage–targeting p97 adaptor that promotes ubiquitin-dependent responses to replication blocks

Mosbech, A., Gibbs‐Seymour, I., Kagias, K., Thorslund, T., Beli, P., Povlsen, L. K., Nielsen, S. V., Smedegaard, S. B., Sedgwick, G. G., Lukas, C., et al. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2395 · Cited by 175 · see citing works

Uncovering SUMOylation Dynamics during Cell-Cycle Progression Reveals FoxM1 as a Key Mitotic SUMO Target Protein

Schimmel, J., Eifler, K., Sigurðsson, J. O., Cuijpers, S. A. G., Hendriks, I. A., Vries, M. V., Kelstrup, C. D., Francavilla, C., Medema, R. H., Olsen, J. V., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.001 · Cited by 175 · see citing works

Comparative Proteomic Analysis Identifies a Role for SUMO in Protein Quality Control

Tatham, M. H., Matić, I., Mann, M., & Hay, R. T. (2011) · Science Signaling · doi:10.1126/scisignal.2001484 · Cited by 175 · see citing works

Usp7 and Uhrf1 control ubiquitination and stability of the maintenance DNA methyltransferase Dnmt1

Qin, W., Leonhardt, H., & Spada, F. (2010) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22998 · Cited by 163 · see citing works

Ubiquitin‐specific proteases 7 and 11 modulate Polycomb regulation of the INK4a tumour suppressor

Maertens, G. N., Messaoudi, S. E., Elderkin, S., Hiom, K. J., & Peters, G. G. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.129 · Cited by 155 · see citing works

Deubiquitination of NF-κB by Ubiquitin-Specific Protease-7 promotes transcription

Colleran, A., Collins, P. E., O’Carroll, C., Ahmed, A., Mao, X., McManus, B., Kiely, P. A., Burstein, E., & Carmody, R. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208446110 · Cited by 150 · see citing works

DVC1 (C1orf124) recruits the p97 protein segregase to sites of DNA damage

Davis, E. J., Lachaud, C., Appleton, P. L., Macartney, T., Näthke, I. S., & Rouse, J. W. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2394 · Cited by 144 · see citing works

SUMO-2 Orchestrates Chromatin Modifiers in Response to DNA Damage

Hendriks, I. A., Treffers, L. W., Vries, M. V., Olsen, J. V., & Vertegaal, A. C. O. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.02.033 · Cited by 136 · see citing works

M phase phosphorylation of the epigenetic regulator UHRF1 regulates its physical association with the deubiquitylase USP7 and stability

Ma, H., Chen, H., Guo, X., Wang, Z., Sowa, M. E., Zheng, L., Hu, S., Zeng, P.-Y., Guo, R., Diao, J., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1116349109 · Cited by 117 · see citing works

Ubiquitin-SUMO Circuitry Controls Activated Fanconi Anemia ID Complex Dosage in Response to DNA Damage

Gibbs‐Seymour, I., Oka, Y., Rajendra, E., Weinert, B. T., Passmore, L. A., Patel, K. J., Olsen, J. V., Choudhary, C., Bekker‐Jensen, S., & Mailand, N. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.12.001 · Cited by 116 · see citing works

An extra allele of Chk1 limits oncogene-induced replicative stress and promotes transformation

Lopez-Contreras, A. J., Gutierrez‐Martinez, P., Specks, J., Rodrigo-Perez, S., & Fernández-Capetillo, Ó. (2012) · The Journal of Experimental Medicine · doi:10.1084/jem.20112147 · Cited by 114 · see citing works

A Proteomic Characterization of Factors Enriched at Nascent DNA Molecules

Lopez-Contreras, A. J., Ruppen, I., Nieto-Soler, M., Murga, M., Rodríguez‐Acebes, S., Remeseiro, S., Rodrigo-Perez, S., Rojas, A. M., Méndez, J., Muñoz, J., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.03.009 · Cited by 114 · see citing works

USP7 counteracts SCFβTrCP- but not APCCdh1-mediated proteolysis of Claspin

Faustrup, H., Bekker-Jensen, S., Bartek, J., Lukas, J., & Mailand, N. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200807137 · Cited by 113 · see citing works

RNF4 and PLK1 are required for replication fork collapse in ATR-deficient cellsPreprint

Ragland, R. L., Patel, S., Rivard, R. S., Smith, K. D., Peters, A. A., Bielinsky, A., & Brown, E. J. (2013) · Genes & Development · doi:10.1101/gad.223180.113 · Cited by 113 · see citing works

Growing sphere of influence: Cdc48/p97 orchestrates ubiquitin-dependent extraction from chromatin

Dantuma, N. P., & Hoppe, T. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.06.003 · Cited by 101 · see citing works

USP7 controls Chk1 protein stability by direct deubiquitination.

Alonso-de Vega, I., Martín, Y., & Smits, V. A. (2014) · Cell Cycle · doi:10.4161/15384101.2014.973324 · Cited by 92 · see citing works

System-wide Analysis of SUMOylation Dynamics in Response to Replication Stress Reveals Novel Small Ubiquitin-like Modified Target Proteins and Acceptor Lysines Relevant for Genome Stability

Xiao, Z., Chang, J.-G., Hendriks, I. A., Sigurðsson, J. O., Olsen, J. V., & Vertegaal, A. C. O. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o114.044792 · Cited by 81 · see citing works

Roles of sequential ubiquitination of PCNA in DNA‐damage tolerance

Zhang, W., Qin, Z., Zhang, X., & Xiao, W. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.04.044 · Cited by 78 · see citing works

Upregulation of Annexin A1 Expression by Butyrate in Human Colon Adenocarcinoma Cells: Role of p53, NF-Y, and p38 Mitogen-Activated Protein Kinase

Lecona, E., Barrasa, J. I., Olmo, N., Llorente, B., Turnay, J., & Lizarbe, M. A. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00650-07 · Cited by 73 · see citing works

Regulation of the Polycomb protein RING1B ubiquitination by USP7

de Bie, P., Zaaroor-Regev, D., & Ciechanover, A. J. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.08.082 · Cited by 71 · see citing works

A role for USP7 in DNA replication.

Jagannathan, M., Nguyen, T., Gallo, D., Luthra, N., Brown, G. W., Saridakis, V., & Frappier, L. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00639-13 · Cited by 71 · see citing works

USP7 modulates UV-induced PCNA monoubiquitination by regulating DNA polymerase eta stability.

Qian, J., Pentz, K., Zhu, Q., Wang, Q., He, J., Srivastava, A. K., & Wani, A. A. (2015) · Oncogene · doi:10.1038/onc.2014.394 · Cited by 61 · see citing works

USP7 Cooperates with SCML2 To Regulate the Activity of PRC1

Lecona, E., Narendra, V. K., & Reinberg, D. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.01197-14 · Cited by 59 · see citing works

Ubiquitin-specific Protease 11 (USP11) Deubiquitinates Hybrid Small Ubiquitin-like Modifier (SUMO)-Ubiquitin Chains to Counteract RING Finger Protein 4 (RNF4)

Hendriks, I. A., Schimmel, J., Eifler, K., Olsen, J. V., & Vertegaal, A. C. O. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.618132 · Cited by 46 · see citing works

Two-way communications between ubiquitin-like modifiers and DNA

Ulrich, H. D. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2805 · Cited by 41 · see citing works

Ubiquitin‐family modifications in the replication of DNA damage

Lehmann, A. R. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.06.005 · Cited by 40 · see citing works

USP7S-dependent inactivation of Mule regulates DNA damage signalling and repair

Khoronenkova, S. V., & Dianov, G. L. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1359 · Cited by 39 · see citing works

Proteome-wide analysis of SUMO2 targets in response to pathological DNA replication stress in human cells

Bursomanno, S., Beli, P., Khan, A. M., Minocherhomji, S., Wagner, S., Bekker‐Jensen, S., Mailand, N., Choudhary, C., Hickson, I. D., & Liu, Y. (2014) · DNA repair · doi:10.1016/j.dnarep.2014.10.011 · Cited by 38 · see citing works

Polycomb Protein SCML2 Regulates the Cell Cycle by Binding and Modulating CDK/CYCLIN/p21 Complexes

Lecona, E., Rojas, L. A., Bonasio, R., Johnston, A. D., Fernández-Capetillo, Ó., & Reinberg, D. (2013) · PLoS Biology · doi:10.1371/journal.pbio.1001737 · Cited by 37 · see citing works

The p150 subunit of CAF-1 causes association of SUMO2/3 with the DNA replication foci

Uwada, J., Tanaka, N., Yamaguchi, Y., Uchimura, Y., Shibahara, K., Nakao, M., & Saitoh, H. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.11.071 · Cited by 20 · see citing works

Regulation of SUMO2 Target Proteins by the Proteasome in Human Cells Exposed to Replication Stress

Bursomanno, S., McGouran, J. F., Kessler, B. M., Hickson, I. D., & Liu, Y. (2015) · Journal of Proteome Research · doi:10.1021/pr500997p · Cited by 12 · see citing works

Mechanisms of Deubiquitinase Specificity and Regulation

Mevissen, T. E. T., & Komander, D. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044916 · Cited by 1,035 · see citing works

Deubiquitylating enzymes and drug discovery: emerging opportunities

Harrigan, J. A., Jacq, X., Martin, N. M., & Jackson, S. P. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.152 · Cited by 940 · see citing works

Signalling mechanisms and cellular functions of SUMO

Vertegaal, A. C. O. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00500-y · Cited by 384 · see citing works

The post-translational modification, SUMOylation, and cancer (Review)

Han, Z., Feng, Y.-H., Gu, B.-H., Li, Y., & Chen, H. (2018) · International Journal of Oncology · doi:10.3892/ijo.2018.4280 · Cited by 337 · see citing works

SUMO-specific proteases and isopeptidases of the SENP family at a glance

Kunz, K., Piller, T., & Müller, S. P. (2018) · Journal of Cell Science · doi:10.1242/jcs.211904 · Cited by 256 · see citing works

SUMO-Mediated Regulation of Nuclear Functions and Signaling Processes

Zhao, X. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.07.027 · Cited by 233 · see citing works

USP7: Structure, substrate specificity, and inhibition

Pozhidaeva, A., & Bezsonova, I. (2019) · DNA Repair · doi:10.1016/j.dnarep.2019.02.005 · Cited by 178 · see citing works

USP1 Is Required for Replication Fork Protection in BRCA1-Deficient Tumors

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Advances in Deubiquitinating Enzyme Inhibition and Applications in Cancer Therapeutics

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Hemi-methylated DNA regulates DNA methylation inheritance through allosteric activation of H3 ubiquitylation by UHRF1

Harrison, J. S., Cornett, E. M., Goldfarb, D., DaRosa, P. A., Li, Z. M., Yan, F., Dickson, B. M., Guo, A. H., Cantu, D. V., Kaustov, L., et al. (2016) · eLife · doi:10.7554/elife.17101 · Cited by 139 · see citing works

USP7: Novel Drug Target in Cancer Therapy

Wang, Z., Kang, W.-T., You, Y., Pang, J., Ren, H., Suo, Z., Liu, H., & Zheng, Y. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00427 · Cited by 124 · see citing works

Functional Analysis of the Replication Fork Proteome Identifies BET Proteins as PCNA Regulators

Wessel, S. R., Mohni, K. N., Luzwick, J. W., Dungrawala, H., & Cortez, D. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.08.051 · Cited by 122 · see citing works

USP7 Is a Master Regulator of Genome Stability

Valles, G. J., Bezsonova, I., Woodgate, R., & Ashton, N. W. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00717 · Cited by 114 · see citing works

A Systems-Level Study Reveals Regulators of Membrane-less Organelles in Human Cells.

Berchtold, D., Battich, N., & Pelkmans, L. (2018) · Molecules and Cells · doi:10.1016/j.molcel.2018.10.036 · Cited by 104 · see citing works

Modulation of the p53/MDM2 interplay by HAUSP inhibitors

Tavana, O., & Gu, W. J. (2016) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjw049 · Cited by 108 · see citing works

USP7 - a crucial regulator of cancer hallmarks

Saha, G., Roy, S., Basu, M., & Ghosh, M. K. (2023) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2023.188903 · Cited by 106 · see citing works

Post-translational Modifications of Key Machinery in the Control of Mitophagy

Wang, L., Qi, H., Tang, Y., & Shen, H. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2019.08.002 · Cited by 102 · see citing works

DNA replication fork speed underlies cell fate changes and promotes reprogramming

Nakatani, T., Lin, J., Ji, F., Ettinger, A. W., Pontabry, J., Tokoro, M., Altamirano‐Pacheco, L., Fiorentino, J., Mahammadov, E., Hatano, Y., et al. (2022) · Nature Genetics · doi:10.1038/s41588-022-01023-0 · Cited by 102 · see citing works

Ubiquitin-dependent and independent roles of SUMO in proteostasis

Liebelt, F., & Vertegaal, A. C. O. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00091.2016 · Cited by 99 · see citing works

Mechanisms of DNA Damage Tolerance: Post-Translational Regulation of PCNA

Leung, W., Baxley, R. M., Moldovan, G., & Bielinsky, A. (2018) · Genes · doi:10.3390/genes10010010 · Cited by 96 · see citing works

Regulation of USP7: A High Incidence of E3 Complexes

Kim, R. Q., & Sixma, T. K. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.05.028 · Cited by 96 · see citing works

Insights in Post-Translational Modifications: Ubiquitin and SUMO

Salas‐Lloret, D., & González‐Prieto, R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23063281 · Cited by 88 · see citing works

Functions of Ubiquitin and SUMO in DNA Replication and Replication Stress

García‐Rodríguez, N., Wong, R. P. C., & Ulrich, H. D. (2016) · Frontiers in Genetics · doi:10.3389/fgene.2016.00087 · Cited by 82 · see citing works

Identification and Characterization of MCM3 as a Kelch-like ECH-associated Protein 1 (KEAP1) Substrate

Mulvaney, K. M., Matson, J. P., Siesser, P. F., Tamir, T. Y., Goldfarb, D., Jacobs, T. M., Cloer, E. W., Harrison, J. S., Vaziri, C., Cook, J. G., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.729418 · Cited by 82 · see citing works

Total chemical synthesis of SUMO-2-Lys63-linked diubiquitin hybrid chains assisted by removable solubilizing tags

Bondalapati, S., Eid, E., Mali, S. M., Wolberger, C., & Brik, A. (2017) · Chemical Science · doi:10.1039/c7sc00488e · Cited by 79 · see citing works

Arabidopsis ubiquitin‐specific proteases UBP12 and UBP13 shape ORE1 levels during leaf senescence induced by nitrogen deficiency

Park, S. H., Jeong, J. S., Seo, J. S., Park, B. S., & Chua, N. (2019) · New Phytologist · doi:10.1111/nph.15879 · Cited by 78 · see citing works

A fork in the road: Where homologous recombination and stalled replication fork protection part ways

Tye, S., Ronson, G. E., & Morris, J. R. (2020) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.07.004 · Cited by 76 · see citing works

SUMO, a small, but powerful, regulator of double-strand break repair

Garvin, A. J., & Morris, J. R. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0281 · Cited by 73 · see citing works

USP25 Regulates the Proliferation and Apoptosis of Ovarian Granulosa Cells in Polycystic Ovary Syndrome by Modulating the PI3K/AKT Pathway via Deubiquitinating PTEN

Gao, Y., Chen, J., Ji, R., Ding, J., Zhang, Y., & Yang, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.779718 · Cited by 74 · see citing works

PARylation prevents the proteasomal degradation of topoisomerase I DNA-protein crosslinks and induces their deubiquitylation

Sun, Y., Chen, J., Huang, S.-Y. N., Su, Y. P., Wang, W., Agama, K., Saha, S. T., Jenkins, L. M. M., Pascal, J. M., & Pommier, Y. G. (2021) · Nature Communications · doi:10.1038/s41467-021-25252-9 · Cited by 70 · see citing works

Global non-covalent SUMO interaction networks reveal SUMO-dependent stabilization of the non-homologous end joining complex

González‐Prieto, R., Eifler, K., Claessens, L. A., Willemstein, E., Xiao, Z., Ormeño, C. M. P. T., Ovaa, H., Ulrich, H. D., & Vertegaal, A. C. O. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108691 · Cited by 68 · see citing works

SUMO-Targeted Ubiquitin Ligases and Their Functions in Maintaining Genome Stability

Chang, Y., Oram, M. K., & Bielinsky, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22105391 · Cited by 64 · see citing works

A TRPV1‐to‐secretagogin regulatory axis controls pancreatic β‐cell survival by modulating protein turnover

Maleńczyk, K., Girach, F., Szodorai, E., Storm, P., Segerstolpe, Å., Tortoriello, G., Schnell, R., Mulder, J., Romanov, R., Borók, E., et al. (2017) · EMBO Journal · doi:10.15252/embj.201695347 · Cited by 60 · see citing works

DUB3 and USP7 de-ubiquitinating enzymes control replication inhibitor Geminin: molecular characterization and associations with breast cancer.

Hernández-Pérez, S., Cabrera, E., Salido, E., Lim, M., Reid, L., Lakhani, S. R., Khanna, K. K., Saunus, J. M., & Freire, R. (2017) · Oncogene · doi:10.1038/onc.2017.21 · Cited by 61 · see citing works

Crystal structure and activity-based labeling reveal the mechanisms for linkage-specific substrate recognition by deubiquitinase USP9X

Paudel, P., Zhang, Q., Leung, C. C. Y., Greenberg, H. C., Guo, Y., Chern, Y.-H., Dong, A., Li, Y., Vedadi, M., Zhuang, Z., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1815027116 · Cited by 59 · see citing works

The USP7 protein interaction network and its roles in tumorigenesis

Al-Eidan, A., Wang, Y., Skipp, P., & Ewing, R. M. (2022) · Genes & Diseases · doi:10.1016/j.gendis.2020.10.004 · Cited by 57 · see citing works

Concerted SUMO-targeted ubiquitin ligase activities of TOPORS and RNF4 are essential for stress management and cell proliferation

Liu, J. C. Y., Ackermann, L., Hoffmann, S., Gál, Z., Hendriks, I. A., Jain, C., Morlot, L., Tatham, M. H., McLelland, G., Hay, R. T., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01294-7 · Cited by 54 · see citing works

USP7 deubiquitinase controls HIV-1 production by stabilizing Tat protein

Ali, A., Raja, R., Farooqui, S. R., Ahmad, S., & Banerjea, A. C. (2017) · Biochemical Journal · doi:10.1042/bcj20160304 · Cited by 54 · see citing works

USP7‐TRIM27 axis negatively modulates antiviral type I IFN signaling

Cai, J., Chen, H., Peng, S., Meng, J., Wang, Y., Zhou, Y. J., Qian, X., Sun, X., Pang, X., Zhang, Y., et al. (2018) · The FASEB Journal · doi:10.1096/fj.201700473rr · Cited by 55 · see citing works

Nuclear deubiquitination in the spotlight: the multifaceted nature of USP7 biology in disease

Rawat, R., Starczynowski, D. T., & Ntziachristos, P. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.02.008 · Cited by 53 · see citing works

Protein deubiquitinase USP7 is required for osteogenic differentiation of human adipose-derived stem cells

Tang, Y., Lv, L., Li, W., Zhang, X., Jiang, Y., Ge, W., & Zhou, Y. (2017) · Stem Cell Research & Therapy · doi:10.1186/s13287-017-0637-8 · Cited by 54 · see citing works

USP1-Trapping Lesions as a Source of DNA Replication Stress and Genomic Instability

Coleman, K. E., Yin, Y., Lui, S. K. L., Keegan, S., Fenyo, D., Smith, D. J., Rothenberg, E., & Huang, T. T. (2022) · Nature Communications · doi:10.1038/s41467-022-29369-3 · Cited by 50 · see citing works

Targeting the DNA damage response and repair in cancer through nucleotide metabolism

Helleday, T., & Rudd, S. G. (2022) · Molecular Oncology · doi:10.1002/1878-0261.13227 · Cited by 48 · see citing works

Paralogue-Specific Roles of SUMO1 and SUMO2/3 in Protein Quality Control and Associated Diseases

Wang, W., & Matunis, M. J. (2023) · Cells · doi:10.3390/cells13010008 · Cited by 45 · see citing works

Chemical Approaches to Intervening in Ubiquitin Specific Protease 7 (USP7) Function for Oncology and Immune Oncology Therapies

Wu, J., Kumar, S., Wang, F., Wang, H., Chen, L., Arsenault, P., Mattern, M. R., & Weinstock, J. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00498 · Cited by 45 · see citing works

SUMO Chains Rule on Chromatin Occupancy

Keiten‐Schmitz, J., Schunck, K., & Müller, S. P. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00343 · Cited by 44 · see citing works

Targeting the USP7/RRM2 axis drives senescence and sensitizes melanoma cells to HDAC/LSD1 inhibitors

Granieri, L., Marocchi, F., Melixetian, M. B., Mohammadi, N., Nicoli, P., Cuomo, A., Bonaldi, T., Confalonieri, S., Pisati, F., Giardina, G., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111396 · Cited by 42 · see citing works

Clinical Significance of Ubiquitin Specific Protease 7 (USP7) in Predicting Prognosis of Hepatocellular Carcinoma and its Functional Mechanisms

Wang, X., Zhang, Q., Wang, Y. K., Zhuang, H., & Chen, B. (2018) · Medical Science Monitor · doi:10.12659/msm.909368 · Cited by 41 · see citing works

USP7 limits CDK1 activity throughout the cell cycle

Galarreta, A., Valledor, P., Ubieto‐Capella, P., Lafarga, V., Zarzuela, E., Muñoz, J., Malumbres, M., Lecona, E., & Fernández-Capetillo, Ó. (2021) · The EMBO Journal · doi:10.15252/embj.201899692 · Cited by 37 · see citing works

Chromatin SUMOylation in heat stress: To protect, pause and organise?

Niskanen, E. A., & Palvimo, J. J. (2017) · BioEssays · doi:10.1002/bies.201600263 · Cited by 39 · see citing works

Inhibition of ubiquitin-specific protease 7 sensitizes acute myeloid leukemia to chemotherapy

Cartel, M., Mouchel, P., Gotanègre, M., David, L., Bertoli, S., Mas, V. M., Besson, A., Sarry, J., Manenti, S., & Didier, C. (2020) · Leukemia · doi:10.1038/s41375-020-0878-x · Cited by 41 · see citing works

The Ubiquitin Ligase TRAIP: Double-Edged Sword at the Replisome

Wu, R., Pellman, D. S., & Walter, J. C. (2020) · Trends in Cell Biology · doi:10.1016/j.tcb.2020.11.007 · Cited by 38 · see citing works

USP7 Regulates Cytokinesis through FBXO38 and KIF20B

Georges, A. A., Coyaud, É., Marcon, E., Greenblatt, J. F., Raught, B., & Frappier, L. (2019) · Scientific Reports · doi:10.1038/s41598-019-39368-y · Cited by 38 · see citing works

Regulation of translesion DNA synthesis in mammalian cells

Ma, X., Tang, T., & Guo, C. (2020) · Environmental and Molecular Mutagenesis · doi:10.1002/em.22359 · Cited by 36 · see citing works

DNA Methylation and Chromatin: Role(s) of Methyl-CpG-Binding Protein ZBTB38

de Dieuleveult, M., & Miotto, B. (2018) · Epigenetics Insights · doi:10.1177/2516865718811117 · Cited by 34 · see citing works

SUMO in the DNA Double-Stranded Break Response: Similarities, Differences, and Cooperation with Ubiquitin

Morris, J. R., & Garvin, A. J. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.05.012 · Cited by 32 · see citing works

Anti-apoptotic effect by the suppression of IRF1 as a downstream of Wnt/β-catenin signaling in colorectal cancer cells

Ohsugi, T., Yamaguchi, K., Zhu, C., Ikenoue, T., Takane, K., Shinozaki, M., Tsurita, G., Yano, H., & Furukawa, Y. (2019) · Oncogene · doi:10.1038/s41388-019-0856-9 · Cited by 34 · see citing works

Ubiquitination and Ubiquitin-Like Modifications in Multiple Myeloma: Biology and Therapy

Wirth, M., Schick, M., Keller, U. B., & Krönke, J. (2020) · Cancers · doi:10.3390/cancers12123764 · Cited by 34 · see citing works

USP7 manipulation by viral proteins

Bojagora, A., & Saridakis, V. (2020) · Virus Research · doi:10.1016/j.virusres.2020.198076 · Cited by 33 · see citing works

Proteomic Analyses of the Eukaryotic Replication Machinery

Cortez, D. (2017) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2017.03.002 · Cited by 31 · see citing works

Timing of DNA lesion recognition: Ubiquitin signaling in the NER pathway

Chitale, S., & Richly, H. (2016) · Cell Cycle · doi:10.1080/15384101.2016.1261227 · Cited by 28 · see citing works

Control of DNA Replication Initiation by Ubiquitin

Hernández-Carralero, E., Cabrera, E., Vega, I. A., Hernández-Pérez, S., Smits, V. A. J., & Freire, R. (2018) · Cells · doi:10.3390/cells7100146 · Cited by 28 · see citing works

Regulation of the Ebola Virus VP24 Protein by SUMO

Vidal, S., Motiam, A. E., Seoane, R., Preitakaitė, V., Bouzaher, Y. H., Gómez-Medina, S., Martín, C. S., Rodríguez, D., Rejas, M. T., Baz-Martínez, M., et al. (2019) · Journal of Virology · doi:10.1128/jvi.01687-19 · Cited by 28 · see citing works

Ubiquitylation at Stressed Replication Forks: Mechanisms and Functions

Mirsanaye, A. S., Typas, D., & Mailand, N. (2021) · Trends in Cell Biology · doi:10.1016/j.tcb.2021.01.008 · Cited by 28 · see citing works

SUMO and the DNA damage response

Bhachoo, J. S., & Garvin, A. J. (2024) · Biochemical Society Transactions · doi:10.1042/bst20230862 · Cited by 27 · see citing works

SUMO enhances unfolding of SUMO–polyubiquitin-modified substrates by the Ufd1/Npl4/Cdc48 complex

Lee, H. G., Lemmon, A. A., & Lima, C. D. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2213703120 · Cited by 26 · see citing works

Functions of SUMO in the Maintenance of Genome Stability

Zilio, N., Eifler, K., & Ulrich, H. D. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-50044-7_4 · Cited by 27 · see citing works

The Ubiquitin-Specific Protease Usp7, a Novel Merkel Cell Polyomavirus Large T-Antigen Interaction Partner, Modulates Viral DNA Replication

Czech‐Sioli, M., Siebels, S., Radau, S., Zahedi, R. P., Schmidt, C., Dobner, T., Grundhoff, A. T., & Fischer, N. (2019) · Journal of Virology · doi:10.1128/jvi.01638-19 · Cited by 26 · see citing works

SUMOylation of Nuclear γ-Actin by SUMO2 supports DNA Damage Repair against Myocardial Ischemia-Reperfusion Injury

Zhao, W., Zhang, X., Zhao, J., Fan, N., & Rong, J. (2022) · International Journal of Biological Sciences · doi:10.7150/ijbs.74407 · Cited by 25 · see citing works

USP7 represses lineage differentiation genes in mouse embryonic stem cells by both catalytic and noncatalytic activities

Liu, C., Sun, L., Tan, Y., Wang, Q. T., Luo, T., Li, C., Yao, N., Xie, Y., Yi, X., Zhu, Y., et al. (2023) · Science Advances · doi:10.1126/sciadv.ade3888 · Cited by 23 · see citing works

USP7 and VCPFAF1 define the SUMO/Ubiquitin landscape at the DNA replication fork

Franz, A., Valledor, P., Ubieto‐Capella, P., Pilger, D., Galarreta, A., Lafarga, V., Fernández-Llorente, A., de la Vega-Barranco, G., den Brave, F., Hoppe, T., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109819 · Cited by 23 · see citing works

Independent functions of DNMT1 and USP7 at replication foci

Yarychkivska, O., Tavana, O., Gu, W. J., & Bestor, T. H. (2018) · Epigenetics & Chromatin · doi:10.1186/s13072-018-0179-z · Cited by 22 · see citing works

Conditional degradation of SDE2 by the Arg/N-End rule pathway regulates stress response at replication forks

Rageul, J., Park, J. J., Jo, U., Weinheimer, A. S., Vu, T. T. M., & Kim, H. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz054 · Cited by 20 · see citing works

Termination of Eukaryotic Replication Forks

Gambus, A. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-6955-0_8 · Cited by 21 · see citing works

Replication Stress: A Review of Novel Targets to Enhance Radiosensitivity-From Bench to Clinic

Zhang, Y., Wu, L., Wang, Z., Wang, J., Roychoudhury, S., Tomasik, B., Wu, G., Wang, G., Rao, X., & Zhou, R. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.838637 · Cited by 21 · see citing works

The SUMOylation and ubiquitination crosstalk in cancer

Li, K., Xia, Y., He, J., Wang, J., Li, J., Ye, M., & Jin, X. (2023) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-023-05310-z · Cited by 20 · see citing works

Ubiquitin and SUMO as timers during DNA replication

Martín-Rufo, R., de la Vega-Barranco, G., & Lecona, E. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.02.013 · Cited by 19 · see citing works

USP7/HAUSP: A SUMO deubiquitinase at the heart of DNA replication

Smits, V. A. J., & Freire, R. (2016) · BioEssays · doi:10.1002/bies.201600096 · Cited by 18 · see citing works

A feedforward circuit shaped by ECT2 and USP7 contributes to breast carcinogenesis

Zhang, Q., Cao, C., Gong, W., Bao, K., Wang, Q., Wang, Y., Bi, L., Ma, S., Zhao, J., Liu, L., et al. (2020) · Theranostics · doi:10.7150/thno.46878 · Cited by 18 · see citing works

Cellular and Molecular Mechanisms of Oxidative DNA Damage and Repair

Ayna, A., Çağlayan, C., & Tayşi, S. (2025) · Medicina · doi:10.3390/medicina61112013 · Cited by 21 · see citing works

Microarray screening reveals two non-conventional SUMO-binding modules linked to DNA repair by non-homologous end-joining

Cabello-Lobato, M. J., Jenner, M., Cisneros‐Aguirre, M., Brüninghoff, K., Sandy, Z., da Costa, I. C., Jowitt, T. A., Loch, C. M., Jackson, S. P., Wu, Q., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac237 · Cited by 17 · see citing works

Structural Basis of the Interaction Between Ubiquitin Specific Protease 7 and Enhancer of Zeste Homolog 2

Gagarina, V., Bojagora, A., Lacdao, I. K., Luthra, N., Pfoh, R., Mohseni, S., Chaharlangi, D., Tan, N., & Saridakis, V. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.12.026 · Cited by 17 · see citing works

PCNA, a focus on replication stress and the alternative lengthening of telomeres pathway

Shen, M. C., Young, A., & Autexier, C. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103055 · Cited by 18 · see citing works

SP1‐activated USP27X‐AS1 promotes hepatocellular carcinoma progression via USP7‐mediated AKT stabilisation

Chen, S., Zhang, H., Mo, J., Liao, Z., Zhang, B., & Zhu, P. (2024) · Clinical and Translational Medicine · doi:10.1002/ctm2.1563 · Cited by 16 · see citing works

A SUMO and ubiquitin code coordinates protein traffic at replication factories

Lecona, E., & Fernández-Capetillo, Ó. (2016) · BioEssays · doi:10.1002/bies.201600129 · Cited by 16 · see citing works

SUMO system – a key regulator in sarcomere organization

Nayak, A., & Amrute‐Nayak, M. (2020) · FEBS Journal · doi:10.1111/febs.15263 · Cited by 16 · see citing works

Systematic identification of factors involved in the silencing of germline genes in mouse embryonic stem cells

Adhami, H. A., Vallet, J., Schaal, C., Schumacher, P., Bardet, A. F., Dumas, M., Chicher, J., Hammann, P., Daujat, S., & Weber, M. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad071 · Cited by 15 · see citing works

Roles of SUMO in Replication Initiation, Progression, and Termination

Wei, L., & Zhao, X. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-6955-0_17 · Cited by 15 · see citing works

Ubiquitin proteomics identifies RNA polymerase I as a target of the Smc5/6 complex

Ibars, E., Codina-Fabra, J., Bellı́, G., Casas, C., Tarrés, M., Solé-Soler, R., Lorite, N. P., Ximénez‐Embún, P., Muñoz, J., Colomina, N., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112463 · Cited by 14 · see citing works

Proteomic strategies for characterizing ubiquitin-like modifications

Li, C., Nelson, T., Vertegaal, A. C. O., & Thibault, P. (2021) · Nature Reviews Methods Primers · doi:10.1038/s43586-021-00048-9 · Cited by 14 · see citing works

Targeting DNA-Protein Crosslinks via Post-Translational Modifications

Leng, X., & Duxin, J. P. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.944775 · Cited by 14 · see citing works

RNF4 sustains Myc-driven tumorigenesis by facilitating DNA replication

Her, J., Zheng, H., & Bunting, S. F. (2024) · Journal of Clinical Investigation · doi:10.1172/jci167419 · Cited by 11 · see citing works

A Survey of Essential Genome Stability Genes Reveals That Replication Stress Mitigation Is Critical for Peri-Implantation Embryogenesis

Kafer, G. R., & Cesare, A. J. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00416 · Cited by 12 · see citing works

Preserving genome integrity: The vital role of SUMO-targeted ubiquitin ligases

Han, J., Mu, Y., & Huang, J. (2023) · Cell Insight · doi:10.1016/j.cellin.2023.100128 · Cited by 11 · see citing works

Improved detection of DNA replication fork-associated proteins

Rivard, R. S., Chang, Y., Ragland, R. L., Thu, Y. M., Kassab, M. A., Mandal, R. S., Riper, S. K. V., Kulej, K., Higgins, L., Markowski, T., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114178 · Cited by 12 · see citing works

SENP3 and USP7 regulate Polycomb-rixosome interactions and silencing functions

Zhou, H., Feng, W., Yu, J., Shafiq, T. A., Paulo, J. A., Zhang, J., Luo, Z., Gygi, S. P., & Moazed, D. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112339 · Cited by 12 · see citing works

The Role of Deubiquitinating Enzyme in Head and Neck Squamous Cell Carcinoma

Jin, S., Kudo, Y., & Horiguchi, T. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010552 · Cited by 11 · see citing works

The deubiquitinating enzyme USP7 regulates the transcription factor Nrf1 by modulating its stability in response to toxic metal exposure

Han, J. J. W., Ho, D. V., Kim, H. M., Lee, J. Y., Jeon, Y. S., & Chan, J. Y. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100732 · Cited by 10 · see citing works

DoUBLing up: ubiquitin and ubiquitin-like proteases in genome stability

Foster, B. M., Wang, Z., & Schmidt, C. K. (2024) · Biochemical Journal · doi:10.1042/bcj20230284 · Cited by 10 · see citing works

RNF4 and USP7 cooperate in ubiquitin-regulated steps of DNA replication

Chang, Y., Lin, K. C., Baxley, R. M., Durrett, W., Wang, L., Stojkova, O., Billmann, M., Ward, H. N., Myers, C. L., & Bielinsky, A. (2023) · Open Biology · doi:10.1098/rsob.230068 · Cited by 9 · see citing works

A SUMO and ubiquitin code coordinates protein traffic at replication factories

Lecona, E., & Fernández-Capetillo, Ó. (2016) · BioEssays · doi:10.1002/bies.201600129 · Cited by 16 · see citing works

BioEssays 9∕2016

(2016) · BioEssays · doi:10.1002/bies.201670085

USP7/HAUSP: A SUMO deubiquitinase at the heart of DNA replication

Smits, V. A. J., & Freire, R. (2016) · BioEssays · doi:10.1002/bies.201600096 · Cited by 18 · see citing works

USP7 and VCPFAF1 define the SUMO/Ubiquitin landscape at the DNA replication fork

Franz, A., Valledor, P., Ubieto‐Capella, P., Pilger, D., Galarreta, A., Lafarga, V., Fernández-Llorente, A., de la Vega-Barranco, G., den Brave, F., Hoppe, T., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109819 · Cited by 23 · see citing works

Regulación de la replicación del ADN por la modificación colectiva del replisoma

Melero, A. P. (2019) · Hispana